Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the disul de isomerase ERp57. The aim of our research is to identify the binding sites for calcitriol in ERp57 and to analyze their interaction. We rst studied the interaction through bioinformatics and uorimetric analyses. Subsequently, we focused on two protein mutants containing the predicted interaction domains with calcitriol: abb’- ERp57, containing the rst three domains, and a’-ERp57, the fourth domain only. To consolidate the achievements we used the calorimetric approach to the whole protein and its mutants. Our results allow us to hypothesize that the interaction with the a’ domain contributes to a greater extent than the other potential binding sites to the dissociation constant, calculated as a Kd of about 10−9 M.
Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 / Gaucci, Elisa; Raimondo, Domenico; Grillo, Caterina; Cervoni, Laura; Altieri, Fabio; Nittari, Giulio; Eufemi, Margherita; Chichiarelli, Silvia. - In: SCIENTIFIC REPORTS. - ISSN 2045-2322. - ELETTRONICO. - 6:(2016), pp. 1-12. [10.1038/srep37957]
Analysis of the interaction of calcitriol with the disulfide isomerase ERp57
GAUCCI, ELISA;RAIMONDO, Domenico;GRILLO, CATERINA;CERVONI, Laura;ALTIERI, Fabio;EUFEMI, Margherita;CHICHIARELLI, Silvia
2016
Abstract
Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the disul de isomerase ERp57. The aim of our research is to identify the binding sites for calcitriol in ERp57 and to analyze their interaction. We rst studied the interaction through bioinformatics and uorimetric analyses. Subsequently, we focused on two protein mutants containing the predicted interaction domains with calcitriol: abb’- ERp57, containing the rst three domains, and a’-ERp57, the fourth domain only. To consolidate the achievements we used the calorimetric approach to the whole protein and its mutants. Our results allow us to hypothesize that the interaction with the a’ domain contributes to a greater extent than the other potential binding sites to the dissociation constant, calculated as a Kd of about 10−9 M.File | Dimensione | Formato | |
---|---|---|---|
Gaucci_analysis_2016.pdf
accesso aperto
Note: Articolo principale
Tipologia:
Versione editoriale (versione pubblicata con il layout dell'editore)
Licenza:
Creative commons
Dimensione
1.14 MB
Formato
Adobe PDF
|
1.14 MB | Adobe PDF |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.